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Volumn 23, Issue 1, 1999, Pages 21-32

Two hemoglobin variants with an alteration of the oxygen-linked chloride binding: Hb antananarivo [α1(NA1)Val→Gly] and Hb Barbizon [β144(HC1)Lys→Met]

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE; GLYCINE; HEMOGLOBIN ANTANANARIVO; HEMOGLOBIN BARBIZON; HEMOGLOBIN VARIANT; LYSINE; METHIONINE; OXYGEN; UNCLASSIFIED DRUG; VALINE;

EID: 0033033561     PISSN: 03630269     EISSN: None     Source Type: Journal    
DOI: 10.3109/03630269908996145     Document Type: Article
Times cited : (9)

References (21)
  • 1
    • 0028245286 scopus 로고
    • The chloride effect in human haemoglobin: A new kind of allosteric mechanism
    • Perutz, M.F., Shih, D.T-b., and Williamson, D.: The chloride effect in human haemoglobin: a new kind of allosteric mechanism. J. Mol. Biol., 239:555-560, 1994.
    • (1994) J. Mol. Biol. , vol.239 , pp. 555-560
    • Perutz, M.F.1    Shih, D.T.-B.2    Williamson, D.3
  • 2
    • 0018572809 scopus 로고
    • X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A
    • O'Donnell, S., Mandaro, R., Schuster, T.M., and Arnone, A.: X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. J. Biol. Chem., 254:12204-12208, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12204-12208
    • O'Donnell, S.1    Mandaro, R.2    Schuster, T.M.3    Arnone, A.4
  • 3
    • 0019332670 scopus 로고
    • Oxygen-linked binding sites for inorganic ions
    • Nigen, A.M., Manning, J.M., and Alben, J.O.: Oxygen-linked binding sites for inorganic ions J. Biol. Chem., 255: 5525-5529, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5525-5529
    • Nigen, A.M.1    Manning, J.M.2    Alben, J.O.3
  • 5
    • 0027453843 scopus 로고
    • A novel allosteric mechanism in haemoglobin: Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin
    • Perutz, M.F., Fermi, G., Poyart, C., Pagnier, J., and Kister J.: A novel allosteric mechanism in haemoglobin: structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. J. Mol. Biol., 233:536-545, 1993.
    • (1993) J. Mol. Biol. , vol.233 , pp. 536-545
    • Perutz, M.F.1    Fermi, G.2    Poyart, C.3    Pagnier, J.4    Kister, J.5
  • 6
    • 0000943392 scopus 로고
    • Electrophoretic mobilities of mutant hemoglobins and mutant globin chains
    • edited by R.M. Schmidt and V.F. Fairbanks, CRC Press, Boca Raton, FL, USA
    • Schneider R.G. and Barwick R.C.: Electrophoretic mobilities of mutant hemoglobins and mutant globin chains. In: CRC Handbook Series in Clinical Laboratory Science, Section I: Hematology, edited by R.M. Schmidt and V.F. Fairbanks, Vol IV, pages 125-139, CRC Press, Boca Raton, FL, USA, 1986.
    • (1986) CRC Handbook Series in Clinical Laboratory Science, Section I: Hematology , vol.4 , pp. 125-139
    • Schneider, R.G.1    Barwick, R.C.2
  • 8
    • 0023609367 scopus 로고
    • Characterization approach of silent beta-chain hemoglobin variants
    • Lacombe, C., Riou, J., Godard, C., Rosa, J., and Galactéros, F.: Characterization approach of silent beta-chain hemoglobin variants. Acta Haematol., 78:119-122, 1986.
    • (1986) Acta Haematol. , vol.78 , pp. 119-122
    • Lacombe, C.1    Riou, J.2    Godard, C.3    Rosa, J.4    Galactéros, F.5
  • 10
    • 0029931313 scopus 로고    scopus 로고
    • Perfusion chromatography on reversed-phase column allows fast analysis of human globin chains
    • Wajcman, H., Ducrocq, R., Riou, J., Mathis, M., Godart, C., Préhu, C., and Galactéros, F.: Perfusion chromatography on reversed-phase column allows fast analysis of human globin chains. Anal. Biochem., 237:80-87, 1996.
    • (1996) Anal. Biochem. , vol.237 , pp. 80-87
    • Wajcman, H.1    Ducrocq, R.2    Riou, J.3    Mathis, M.4    Godart, C.5    Préhu, C.6    Galactéros, F.7
  • 11
    • 0027729406 scopus 로고
    • Structural characterization of abnormal hemoglobins from dried blood specimens in a neonatal screening program
    • Wajcman, H., Bardakdjian, J., and Ducrocq, R.: Structural characterization of abnormal hemoglobins from dried blood specimens in a neonatal screening program. Ann. Biol. Clin., 51:867-870, 1993.
    • (1993) Ann. Biol. Clin. , vol.51 , pp. 867-870
    • Wajcman, H.1    Bardakdjian, J.2    Ducrocq, R.3
  • 12
    • 0030822728 scopus 로고    scopus 로고
    • Combining mass spectrometry methods allows characterization of human hemoglobin variants localized within αT9 peptide: Identification of Hb Villeurbanne α89 (FG1) His→Tyr
    • Déon, C., Promé, J.C., Promé, D., Francina, A., Groff, P., Kalmes, G., Galactéros, F., and Wajcman, H.: Combining mass spectrometry methods allows characterization of human hemoglobin variants localized within αT9 peptide: identification of Hb Villeurbanne α89 (FG1) His→Tyr. J. Mass Spectrom., 32:880-887, 1997.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 880-887
    • Déon, C.1    Promé, J.C.2    Promé, D.3    Francina, A.4    Groff, P.5    Kalmes, G.6    Galactéros, F.7    Wajcman, H.8
  • 13
    • 0023257012 scopus 로고
    • An expanded two-state allosteric model for interaction of human hemoglobin A with non saturating concentrations of 2,3 diphosphoglycerate
    • Kister, J., Poyart, C., and Edelstein, S.J.: An expanded two-state allosteric model for interaction of human hemoglobin A with non saturating concentrations of 2,3 diphosphoglycerate. J. Biol. Chem., 252:12085-12091, 1987.
    • (1987) J. Biol. Chem. , vol.252 , pp. 12085-12091
    • Kister, J.1    Poyart, C.2    Edelstein, S.J.3
  • 14
    • 0026785750 scopus 로고
    • Allosteric modifiers of hemoglobin: 2-[4-[[(3,5-disubstituted anilino) carbonyl] methyl] phenoxy]-2-methylpropionic acid derivatives that lower the oxygen affinity of hemoglobin in red cell suspensions, in whole blood, and in vivo in rats
    • Abraham, D.J., Wireko, F.C., Randad, R.S., Poyart, C., Kister, J., Bohn, B., Liard, J-F., and Kunert, M.P.: Allosteric modifiers of hemoglobin: 2-[4-[[(3,5-disubstituted anilino) carbonyl] methyl] phenoxy]-2-methylpropionic acid derivatives that lower the oxygen affinity of hemoglobin in red cell suspensions, in whole blood, and in vivo in rats. Biochemistry, 31: 9141-9149, 1992.
    • (1992) Biochemistry , vol.31 , pp. 9141-9149
    • Abraham, D.J.1    Wireko, F.C.2    Randad, R.S.3    Poyart, C.4    Kister, J.5    Bohn, B.6    Liard, J.-F.7    Kunert, M.P.8
  • 15
    • 0023899659 scopus 로고
    • Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin
    • Boissel, J.P., Kasper, T.J., and Bunn, H.F.: Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin. J. Biol. Chem., 263:8443-8449, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8443-8449
    • Boissel, J.P.1    Kasper, T.J.2    Bunn, H.F.3
  • 16
    • 0016350545 scopus 로고
    • 2 144 Lys→Asn: A new high-oxygen-affinity mutant human hemoglobin
    • 2 144 Lys→Asn: a new high-oxygen-affinity mutant human hemoglobin. Blood, 44:543-549, 1974.
    • (1974) Blood , vol.44 , pp. 543-549
    • Zak, S.J.1    Brimhall, B.2    Jones, R.T.3    Kaplan, M.E.4
  • 17
    • 0022375048 scopus 로고
    • A new hemoglobin variant, Hb Mito [β144 (HCl) Lys→Glu], with increased oxygen affinity
    • Harano, K., Harano, T., Ueda, S., Ohkushi, T., and Imai, K.: A new hemoglobin variant, Hb Mito [β144 (HCl) Lys→Glu], with increased oxygen affinity. FEBS Letters, 192:75-78, 1985.
    • (1985) FEBS Letters , vol.192 , pp. 75-78
    • Harano, K.1    Harano, T.2    Ueda, S.3    Ohkushi, T.4    Imai, K.5
  • 19
    • 0029120990 scopus 로고
    • Interaction of two amino acid substitutions within the same β chain of human hemoglobin: The examples of Hb Corbeil [β26(B8)Glu→Lys, β104(G6)Arg→Thr] and Hb Villeparisis [β77(EF1) His→Tyr, β80(EF4)Asn→Ser]
    • Wajcman, H., Kister, J., Promé, D., Blouquit, Y., Préhu, C., Poyart, C., and Galactéros, F.: Interaction of two amino acid substitutions within the same β chain of human hemoglobin: the examples of Hb Corbeil [β26(B8)Glu→Lys, β104(G6)Arg→Thr] and Hb Villeparisis [β77(EF1) His→Tyr, β80(EF4)Asn→Ser]. Comptes Rendus Acad. Sci. Paris, Sciences de la vie/Life sciences, 318:785-794, 1995.
    • (1995) Comptes Rendus Acad. Sci. Paris, Sciences de la Vie/Life Sciences , vol.318 , pp. 785-794
    • Wajcman, H.1    Kister, J.2    Promé, D.3    Blouquit, Y.4    Préhu, C.5    Poyart, C.6    Galactéros, F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.